AMCY_PARDE
ID AMCY_PARDE Reviewed; 131 AA.
AC P22364;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Amicyanin;
DE Flags: Precursor;
GN Name=mauC; Synonyms=ami;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19367 / NBRC 13301 / NCIMB 8944 / NRRL B-3785;
RX PubMed=2261991; DOI=10.1016/0014-5793(90)81475-4;
RA van Spanning R.J.M., Wansell C.W., Reijnders W.N.M., Oltmann L.F.,
RA Stouthamer A.H.;
RT "Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and
RT the resultant effect on methylamine oxidation.";
RL FEBS Lett. 275:217-220(1990).
RN [2]
RP PROTEIN SEQUENCE OF 27-36.
RX PubMed=3718960; DOI=10.1021/bi00357a020;
RA Husain M., Davidson V.L.;
RT "Properties of Paracoccus denitrificans amicyanin.";
RL Biochemistry 25:2431-2436(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH MADH.
RX PubMed=1599920; DOI=10.1021/bi00136a006;
RA Chen L., Durley R., Poliks B.J., Hamada K., Chen Z., Mathews F.S.,
RA Davidson V.L., Satow Y., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.;
RT "Crystal structure of an electron-transfer complex between methylamine
RT dehydrogenase and amicyanin.";
RL Biochemistry 31:4959-4964(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8140419; DOI=10.1126/science.8140419;
RA Chen L., Durley R., Mathews F.S., Davidson V.L.;
RT "Structure of an electron transfer complex: methylamine dehydrogenase,
RT amicyanin, and cytochrome c551i.";
RL Science 264:86-90(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS).
RX PubMed=15299631; DOI=10.1107/s0907444996001072;
RA Cunane L.M., Chen Z.-W., Durley R.C.E., Mathews F.S.;
RT "X-ray structure of the cupredoxin amicyanin, from Paracoccus
RT denitrificans, refined at 1.31-A resolution.";
RL Acta Crystallogr. D 52:676-686(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), AND COPPER-BINDING SITES HIS-79;
RP CYS-118; HIS-121 AND MET-124.
RX PubMed=9860825; DOI=10.1021/bi9817919;
RA Zhu Z., Cunane L.M., Chen Z.-W., Durley R.C.E., Mathews F.S.,
RA Davidson V.L.;
RT "Molecular basis for interprotein complex-dependent effects on the redox
RT properties of amicyanin.";
RL Biochemistry 37:17128-17136(1998).
CC -!- FUNCTION: Primary acceptor of electrons from methylamine dehydrogenase.
CC Passes those electrons on either a soluble cytochrome c or to
CC pseudoazurin.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 1 copper ion per subunit.;
CC -!- PATHWAY: One-carbon metabolism; methylamine degradation.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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DR EMBL; X55665; CAA39199.1; -; Genomic_DNA.
DR PIR; A24407; A24407.
DR PIR; S12972; S12972.
DR PDB; 1AAC; X-ray; 1.31 A; A=27-131.
DR PDB; 1AAJ; X-ray; 1.80 A; A=27-131.
DR PDB; 1AAN; X-ray; 2.00 A; A=27-131.
DR PDB; 1BXA; X-ray; 1.30 A; A=27-131.
DR PDB; 1MDA; X-ray; 2.50 A; A/B=29-131.
DR PDB; 1MG2; X-ray; 2.25 A; C/G/K/O=27-131.
DR PDB; 1MG3; X-ray; 2.40 A; C/G/K/O=27-131.
DR PDB; 1SF3; X-ray; 1.05 A; A=27-131.
DR PDB; 1SF5; X-ray; 1.10 A; A=27-131.
DR PDB; 1SFD; X-ray; 0.99 A; A/B=27-131.
DR PDB; 1SFH; X-ray; 1.05 A; A/B=27-131.
DR PDB; 1T5K; X-ray; 1.40 A; A/B/C/D=27-131.
DR PDB; 2GB2; X-ray; 1.25 A; A=27-131.
DR PDB; 2GBA; X-ray; 0.92 A; A=27-131.
DR PDB; 2GC4; X-ray; 1.90 A; C/G/K/O=27-131.
DR PDB; 2GC7; X-ray; 1.90 A; C/G/K/O=27-131.
DR PDB; 2IDQ; X-ray; 0.90 A; A=27-131.
DR PDB; 2IDS; X-ray; 1.00 A; A=27-131.
DR PDB; 2IDT; X-ray; 1.00 A; A=27-131.
DR PDB; 2IDU; X-ray; 0.95 A; A=27-131.
DR PDB; 2J55; X-ray; 2.15 A; A/B=27-131.
DR PDB; 2J56; X-ray; 2.10 A; A/B=27-131.
DR PDB; 2J57; X-ray; 2.25 A; A/B/C/D=27-131.
DR PDB; 2MTA; X-ray; 2.40 A; A=27-131.
DR PDB; 2OV0; X-ray; 0.75 A; A=27-131.
DR PDB; 2QDV; X-ray; 0.89 A; A=27-131.
DR PDB; 2QDW; X-ray; 0.92 A; A=27-131.
DR PDB; 2RAC; X-ray; 1.30 A; A=27-131.
DR PDB; 3IE9; X-ray; 2.10 A; A=27-131.
DR PDB; 3IEA; X-ray; 2.20 A; A=27-131.
DR PDB; 3L45; Other; 1.80 A; A=27-131.
DR PDB; 3PLY; X-ray; 2.20 A; A/B/C/D=27-131.
DR PDB; 3RYM; X-ray; 1.70 A; A/B/C/D=27-131.
DR PDB; 4P5R; X-ray; 1.09 A; A=27-131.
DR PDB; 4P5S; X-ray; 1.02 A; A=27-131.
DR PDBsum; 1AAC; -.
DR PDBsum; 1AAJ; -.
DR PDBsum; 1AAN; -.
DR PDBsum; 1BXA; -.
DR PDBsum; 1MDA; -.
DR PDBsum; 1MG2; -.
DR PDBsum; 1MG3; -.
DR PDBsum; 1SF3; -.
DR PDBsum; 1SF5; -.
DR PDBsum; 1SFD; -.
DR PDBsum; 1SFH; -.
DR PDBsum; 1T5K; -.
DR PDBsum; 2GB2; -.
DR PDBsum; 2GBA; -.
DR PDBsum; 2GC4; -.
DR PDBsum; 2GC7; -.
DR PDBsum; 2IDQ; -.
DR PDBsum; 2IDS; -.
DR PDBsum; 2IDT; -.
DR PDBsum; 2IDU; -.
DR PDBsum; 2J55; -.
DR PDBsum; 2J56; -.
DR PDBsum; 2J57; -.
DR PDBsum; 2MTA; -.
DR PDBsum; 2OV0; -.
DR PDBsum; 2QDV; -.
DR PDBsum; 2QDW; -.
DR PDBsum; 2RAC; -.
DR PDBsum; 3IE9; -.
DR PDBsum; 3IEA; -.
DR PDBsum; 3L45; -.
DR PDBsum; 3PLY; -.
DR PDBsum; 3RYM; -.
DR PDBsum; 4P5R; -.
DR PDBsum; 4P5S; -.
DR AlphaFoldDB; P22364; -.
DR BMRB; P22364; -.
DR SMR; P22364; -.
DR IntAct; P22364; 3.
DR DrugBank; DB02467; L-methionine (S)-S-oxide.
DR DrugBank; DB08646; TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OL.
DR OMA; CTPHPFM; -.
DR UniPathway; UPA00895; -.
DR EvolutionaryTrace; P22364; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd13921; Amicyanin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR035668; Amicyanin.
DR InterPro; IPR002386; Amicyanin/Pseudoazurin.
DR InterPro; IPR013475; Amicyanin_Para/Methyl.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR001235; Copper_blue_Plastocyanin.
DR InterPro; IPR008972; Cupredoxin.
DR Pfam; PF00127; Copper-bind; 1.
DR PRINTS; PR00155; AMICYANIN.
DR PRINTS; PR00156; COPPERBLUE.
DR SUPFAM; SSF49503; SSF49503; 1.
DR TIGRFAMs; TIGR02657; amicyanin; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Electron transport;
KW Metal-binding; Periplasm; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:3718960"
FT CHAIN 27..131
FT /note="Amicyanin"
FT /id="PRO_0000002844"
FT DOMAIN 27..131
FT /note="Plastocyanin-like"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 124
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2OV0"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2OV0"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:2OV0"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2OV0"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2OV0"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2OV0"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2OV0"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2OV0"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:2OV0"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2OV0"
SQ SEQUENCE 131 AA; 13983 MW; F7352A865FD089DA CRC64;
MISATKIRSC LAACVLAAFG ATGALADKAT IPSESPFAAA EVADGAIVVD IAKMKYETPE
LHVKVGDTVT WINREAMPHN VHFVAGVLGE AALKGPMMKK EQAYSLTFTE AGTYDYHCTP
HPFMRGKVVV E
